In eukaryotic cells, DNA is wrapped around histone proteins to form the basic repeating unit of chromatin, the nucleosome core particle. Most nucleosomes consist of two copies each of histones: H2A and H2B in a heterodimer and histones H3 and H4 in a heterotetramer. Because of their intimate association with DNA, histones regulate all DNA-templated processes including transcription, DNA replication, and DNA damage response and repair. Several studies have highlighted the importance of a small portion of the histone H2A N-terminal domain which regulates global transcription. This domain is responsible for the repression of about 5% of yeast genes. This domain, termed the histone H2A Repression (H.A.R.) domain, consists of a well-conserved region of histone H2A. The H.A.R. domain has also been shown to be an important regulator of DNA damage response and repair. In this study, we show that the H.A.R. domain has a distinct role in DNA replication. Using a high-throughput spotting assay, we found that deletion of the H.A.R. domain leads to a marked sensitivity to hydroxyurea. We also show differential expression of genes involved in regulating DNA replication (e.g. the ribonucleotide reductase genes), in the absence and presence of hydroxyurea. Finally, we show that H.A.R. mutants show distinct delays in cell cycle progression relative to wild-type. Taken together these data suggest a novel function of the H.A.R. domain in regulating cell cycle progression.

Histone H2A N-terminal domain regulates cell cycle progression in the yeast Saccharomyces cerevisiae

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.